TECTA_CHICK
ID TECTA_CHICK Reviewed; 2120 AA.
AC Q9YH85;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha-tectorin;
DE Flags: Precursor;
GN Name=TECTA;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Cochlear duct;
RX PubMed=10320099; DOI=10.1016/s0378-5955(98)00213-5;
RA Coutinho P., Goodyear R., Legan P.K., Richardson G.P.;
RT "Chick alpha-tectorin: molecular cloning and expression during
RT embryogenesis.";
RL Hear. Res. 130:62-74(1999).
RN [2]
RP PROTEIN SEQUENCE OF 25-33; 325-334 AND 1105-1124.
RX PubMed=9079715; DOI=10.1074/jbc.272.13.8791;
RA Legan P.K., Rau A., Keene J.N., Richardson G.P.;
RT "The mouse tectorins. Modular matrix proteins of the inner ear homologous
RT to components of the sperm-egg adhesion system.";
RL J. Biol. Chem. 272:8791-8801(1997).
RN [3]
RP FUNCTION.
RX PubMed=1490898; DOI=10.1016/0378-5955(92)90165-j;
RA Killick R., Malenczak C., Richardson G.P.;
RT "The protein composition of the avian tectorial membrane.";
RL Hear. Res. 64:21-38(1992).
CC -!- FUNCTION: One of the major non-collagenous components of the tectorial
CC membrane. The tectorial membrane is an extracellular matrix of the
CC inner ear that covers the neuroepithelium of the cochlea and contacts
CC the stereocilia bundles of specialized sensory hair cells. Sound
CC induces movement of these hair cells relative to the tectorial
CC membrane, deflects the stereocilia and leads to fluctuations in hair-
CC cell membrane potential, transducing sound into electrical signals.
CC {ECO:0000269|PubMed:1490898}.
CC -!- SUBUNIT: May form homomeric filament after self-association or
CC heteromeric filament after association with beta-tectorin.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted,
CC extracellular space, extracellular matrix. Note=Found in the non-
CC collagenous matrix of the tectorial membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the inner ear.
CC {ECO:0000269|PubMed:10320099}.
CC -!- DEVELOPMENTAL STAGE: Apically located within the epithelium of the
CC developing basilar papilla at days E5.5 to E8. As development proceeds,
CC expression becomes restricted to the basal layer. In the utricle,
CC alpha-tectorin is first expressed at E4.5.
CC {ECO:0000269|PubMed:10320099}.
CC -!- DOMAIN: Zona pellucida domain may enable to form filaments.
CC -!- PTM: At least 3 products of tectorin seem to exist: HMM, MMM and LMM.
CC They may be generated by active processing or the result of proteolysis
CC occurring between intrachain disulfide bonds.
CC -!- PTM: The presence of a hydrophobic C-terminus preceded by a potential
CC cleavage site strongly suggests that tectorins are synthesized as
CC glycosylphosphatidylinositol-linked, membrane-bound precursors.
CC Tectorins are targeted to the apical surface of the inner ear epithelia
CC by the lipid and proteolytically released into the extracellular
CC compartment.
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DR EMBL; AJ012287; CAA09979.1; -; mRNA.
DR PIR; T30243; T30243.
DR AlphaFoldDB; Q9YH85; -.
DR SMR; Q9YH85; -.
DR STRING; 9031.ENSGALP00000040065; -.
DR VEuPathDB; HostDB:geneid_395686; -.
DR eggNOG; KOG1216; Eukaryota.
DR eggNOG; KOG4291; Eukaryota.
DR InParanoid; Q9YH85; -.
DR PhylomeDB; Q9YH85; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR033026; TECTA.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR025615; TILa_dom.
DR InterPro; IPR014853; Unchr_dom_Cys-rich.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR PANTHER; PTHR46160:SF3; PTHR46160:SF3; 1.
DR Pfam; PF08742; C8; 3.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF01826; TIL; 3.
DR Pfam; PF12714; TILa; 1.
DR Pfam; PF00094; VWD; 4.
DR Pfam; PF00100; Zona_pellucida; 1.
DR SMART; SM00832; C8; 3.
DR SMART; SM00539; NIDO; 1.
DR SMART; SM00215; VWC_out; 2.
DR SMART; SM00216; VWD; 4.
DR SMART; SM00241; ZP; 1.
DR SUPFAM; SSF57567; SSF57567; 3.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS51233; VWFD; 4.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; GPI-anchor; Hearing; Lipoprotein;
KW Membrane; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:9079715"
FT CHAIN 25..2058
FT /note="Alpha-tectorin"
FT /id="PRO_0000041739"
FT PROPEP 2059..2120
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041740"
FT DOMAIN 98..252
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 260..312
FT /note="VWFC"
FT DOMAIN 317..490
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 578..620
FT /note="TIL 1"
FT DOMAIN 690..865
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 963..1013
FT /note="TIL 2"
FT DOMAIN 1066..1250
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1345..1398
FT /note="TIL 3"
FT DOMAIN 1458..1633
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1772..2026
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT LIPID 2058
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 834
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 928
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1025
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1041
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1739
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1831
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1847
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1906
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 319..451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 341..489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 692..828
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1068..1213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1090..1249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1460..1594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1482..1632
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1684..1742
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 1708..1751
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 1753..1785
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 1773..1865
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 1804..1824
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 1947..2007
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1968..2023
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT DISULFID 2012..2019
FT /evidence="ECO:0000250|UniProtKB:P07911"
FT CONFLICT 1114..1115
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1123
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2120 AA; 233965 MW; E93F69EA18B51A4C CRC64;
MNTRSLLSAW AALLVVTVRH RAHAMASLYP FWPNDTKTPK VDDGSSSEIK LSVPFIFFRS
PYRTVYVNNN GVISFNSLVS QFTPEAFPLA DGRAFVAPFC GDVANGIRGE IYYRESTNPE
LLGESSKDIR KYFKDMASFS ASWVFIVTWE EVQFYGGSST TPVNTFQAVL ITDGVSSFAI
FNYQEISWTT GTASGGDPLT GLGGVMAQAG FNGGNISNFF SIPGSRTPDI VNIEQTTNVN
IPGRWAFKID GREIDPANLS LRGQFLHQGE IFWENSNCST KCRCLDFNNE IFCQEMLAPF
ETVEPKIKFF QCVPVETACV VFGDPHYHTF DGFLFHFQGS CSYLLARQCW PGSQLPYFNV
EAKNERGGSS VSWAEDIFVE VYRHKIVLPK GGFGKAKVDD LVVSLGAIKV YQSGLSTALE
TDFGLLVTYD GQHYASVSVP GTYINGTCGL CGNYNKDPED DALRSDGRLA SSVPELGESW
RVPHPERKCS PGCVENCSVC DASRILYSPI CGFSQECGAW SVLVATAFVH SCVYDLCSAR
RTHRLCQAIQ VTLRCCQGLG IRWENGVPDG MRGGLAVPGH SHYSGCASGC PATCSDLTAP
LRCTAPCPEG CECDDGHVLS ARPLHSLCRS GCVVDGRSRC REVFWATADC TAECQCEDGG
EAKCFNTSCP EGEVCTIEDG YRGCYPKREG LCSVGQNQVL RTFDGVTFPY PLEHSYTLLK
TCMEKPDFIE VDISQKKPDT LPMAGRVVRI QVVGQEVKVG GASLSEVKVN GYDVDLPYFH
PSGHLEIYRT DNGTVTESEG LLSIGYYDSG LLEIRLSTAY FNCTGGLCGF FNGNDSDEFC
TPKAKCTDNL ELFLESWTTF DEICNGECGD LLKACNNDSE LLKTYRSRSN CAIINDPTNS
SFLECHNVSI VSAYYRTCLF RLCQSGGNQS ELCSAVARYA SACKNSEVDV GQWRSHSFCP
LACPENSHFE ECMSCVETCE TLATGCCMDT CTEGCQCDEG FALRSPCVPR GECGCNFEGH
ELATNQTFWM DISCHLLCYC NGSDNSVYCE NVLQDDEYYC HVRTDASCIV SGYGHYLTFD
GFSFDFQSSC ALVLCTTIHG ACERSDTFPT FTVTVTAKNE DRDTSLACVV KQVEVEVFNY
YIVIHRAYKY TVMINNERLY LPLKLGQGKV NIFAFGFHIV VETDFGLKVV YDWKTFLSVT
IPRSFQNLTY GLCGRYNGNP DDDLVAAGGT PRFGVTDFVQ SWAKRDTFCR VGSGDRCPAC
GKVEGFWKPQ QLCSLIPSQS GVFAKCHSKI NPSYFYKNCL FDTVVDGGAM ARRVADWLQN
YASTCQTQGI AIIGWRNFTS CSVSCPPNSH YESCVSLCQP RCAAIRLKSD CGHYCVEGCQ
CDPGYVLNGK SCILPQNCGC YSDGKYYEPK QLFWNGDCTR RCARFRRNLI QCDPRHCKSD
EECASRNGVR GCFSTRSSFC LAAGGGVFRT FDGAFLRFPA NCAFVLSTIC QRLADFSFQL
IINFDKWSSP NLTIISVYIY INEEQILISD RSTVKVNGSL VSIPFVTGLS TKIYSQEGFL
VIDSGPDIHI RYNGFNVIKI TIGDRLQNKV CGLCGNFNGD PADDYATLRG KPVVSSVVLA
QSWKTNGMQK SCNELQYSQY AASCDNVQIQ KLQSDSYCLK LTDMKGFFQP CYGLLDPLPF
YESCFLDGCY NRKQVQLCGS LAAYGEACRT FGILGTEWIE KENCSGVVED PCAGADCPNR
TCELDDGGEL CGCIEPPPYG NTTHDIIDAE VTCKAAQMEV SISKCKLFQL GFEREGVRVN
DRHCPGIEGE DFISFQINNT KGNCGNLVQS NSTHIVYKNT VWIESANNTG NIITRDRTIN
VEVFCAYELD IKISLDSVVR PMLSVINLTV PTQEGSFTTK MALYKNSSYK HPYRQGEVVL
TTRDVLYVGV FVVGADSNHL ILMLNKCYAT PSRDSNDKLR YFIIEGGCQN LKDNTIGIEE
NGVSLTCRFH VTVFKFIGDY DEVHLHCAVS LCDSEKYSCK INCPQHRRSA SAFAQEAHEQ
ILSVGPIRRK RSDWCEDNGG CEQICTSQAD GPLCSCVTGT LQGDGKSCMA SSSSADIRAQ
ASLLVAAQLW LWAALHDPTS
